ID   ETV3_PANTR              Reviewed;         512 AA.
AC   A2T762;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2007, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=ETS translocation variant 3;
GN   Name=ETV3;
OS   Pan troglodytes (Chimpanzee).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pan.
OX   NCBI_TaxID=9598;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Nickel G.C., Tefft D.L., Trevarthen K., Funt J., Adams M.D.;
RT   "Positive selection in transcription factor genes on the human lineage.";
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Transcriptional repressor that contribute to growth arrest
CC       during terminal macrophage differentiation by repressing target genes
CC       involved in Ras-dependent proliferation. Represses MMP1 promoter
CC       activity (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00237}.
CC   -!- SIMILARITY: Belongs to the ETS family. {ECO:0000305}.
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DR   EMBL; DQ977379; ABM92017.1; -; Genomic_DNA.
DR   RefSeq; NP_001074948.1; NM_001081479.1.
DR   RefSeq; XP_009432030.1; XM_009433755.2.
DR   RefSeq; XP_009432034.1; XM_009433759.2.
DR   AlphaFoldDB; A2T762; -.
DR   SMR; A2T762; -.
DR   STRING; 9598.ENSPTRP00000002513; -.
DR   PaxDb; A2T762; -.
DR   Ensembl; ENSPTRT00000095701; ENSPTRP00000071945; ENSPTRG00000049741.
DR   GeneID; 457412; -.
DR   KEGG; ptr:457412; -.
DR   CTD; 2117; -.
DR   VGNC; VGNC:11313; ETV3.
DR   eggNOG; KOG3806; Eukaryota.
DR   GeneTree; ENSGT00940000160963; -.
DR   HOGENOM; CLU_023454_1_0_1; -.
DR   InParanoid; A2T762; -.
DR   OMA; GIYPDPH; -.
DR   OrthoDB; 677533at2759; -.
DR   TreeFam; TF351065; -.
DR   Proteomes; UP000002277; Chromosome 1.
DR   Bgee; ENSPTRG00000049741; Expressed in temporal lobe and 21 other tissues.
DR   GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR   GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IEA:InterPro.
DR   GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IEA:Ensembl.
DR   GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   Gene3D; 1.10.10.10; -; 1.
DR   InterPro; IPR000418; Ets_dom.
DR   InterPro; IPR046328; ETS_fam.
DR   InterPro; IPR032929; ETV3.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   PANTHER; PTHR11849; PTHR11849; 1.
DR   PANTHER; PTHR11849:SF30; PTHR11849:SF30; 1.
DR   Pfam; PF00178; Ets; 1.
DR   PRINTS; PR00454; ETSDOMAIN.
DR   SMART; SM00413; ETS; 1.
DR   SUPFAM; SSF46785; SSF46785; 1.
DR   PROSITE; PS00345; ETS_DOMAIN_1; 1.
DR   PROSITE; PS00346; ETS_DOMAIN_2; 1.
DR   PROSITE; PS50061; ETS_DOMAIN_3; 1.
PE   3: Inferred from homology;
KW   Acetylation; DNA-binding; Isopeptide bond; Nucleus; Phosphoprotein;
KW   Reference proteome; Repressor; Transcription; Transcription regulation;
KW   Ubl conjugation.
FT   CHAIN           1..512
FT                   /note="ETS translocation variant 3"
FT                   /id="PRO_0000285523"
FT   DNA_BIND        35..116
FT                   /note="ETS"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00237"
FT   REGION          136..222
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          336..512
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        152..185
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        186..202
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        382..420
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        450..490
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         139
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P41162"
FT   MOD_RES         159
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P41162"
FT   MOD_RES         315
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8R4Z4"
FT   MOD_RES         388
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P41162"
FT   CROSSLNK        381
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P41162"
FT   CROSSLNK        388
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2); alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P41162"
SQ   SEQUENCE   512 AA;  57131 MW;  35F75EEEA28B120D CRC64;
     MKAGCSIVEK PEGGGGYQFP DWAYKTESSP GSRQIQLWHF ILELLQKEEF RHVIAWQQGE
     YGEFVIKDPD EVARLWGRRK CKPQMNYDKL SRALRYYYNK RILHKTKGKR FTYKFNFNKL
     VMPNYPFINI RSSGVVPQSA PPVPTASSRF HFPPLDTHSP TNDVQPGRFS ASSLTASGQE
     SSNGTDRKTE LSELEDGSAA DWRRGVDPMS SRNAIGGGGI GHQKRKPDIM LPLFARPGMY
     PDPHSPFAVS PIPGRGGVLN VPISPALSLT PTIFSYSPSP GLSPFTSSSC FSFNPEEMKH
     YLHSQACSVF NYHLSPRTFP RYPGLMVPPL QCQMHPEEST QFSIKLQPPP VGRKNRERVE
     SSEESAPVTT PTMASIPPRI KVEPASEKDP ESLRQSAREK EEHTQEEGTV PSRTIEEEKG
     TIFARPAAPP IWPSVPISTP SEEPLEVTED IEDRPGKEPS APEKKEDALM PPKLRLKRRW
     NDDPEARELS KSGKFLWNGS GPQGLATAAA DA